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Titolo:
An acid amidase hydrolyzing anandamide as an endogenous ligand for cannabinoid receptors
Autore:
Ueda, N; Yamanaka, K; Terasawa, Y; Yamamoto, S;
Indirizzi:
Univ Tokushima, Sch Med, Dept Biochem, Tokushima 7708503, Japan Univ Tokushima Tokushima Japan 7708503 Biochem, Tokushima 7708503, Japan
Titolo Testata:
FEBS LETTERS
fascicolo: 3, volume: 454, anno: 1999,
pagine: 267 - 270
SICI:
0014-5793(19990709)454:3<267:AAAHAA>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAT-BRAIN; CELL-LINE; PHENYLMETHYLSULFONYL FLUORIDE; MOLECULAR CHARACTERIZATION; AMIDOHYDROLASE; BINDING; ENZYME; IDENTIFICATION; DEGRADATION; INHIBITOR;
Keywords:
cannabinoid; anandamide; palmitoylethanolamide; fatty acid amide hydrolase; megakaryoblastic cell;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Yamamoto, S Univ Tokushima, Sch Med, Dept Biochem, Kuramoto Cho, Tokushima7708503, Japan Univ Tokushima Kuramoto Cho Tokushima Japan 7708503 03, Japan
Citazione:
N. Ueda et al., "An acid amidase hydrolyzing anandamide as an endogenous ligand for cannabinoid receptors", FEBS LETTER, 454(3), 1999, pp. 267-270

Abstract

Anandamide loses its cannabimimetic activities upon hydrolysis to arachidonic acid and ethanolamine. So far the anandamide hydrolyzing activity widely distributed in mammalian organs has been attributed exclusively to an enzyme referred to as anandamide amidohydrolase with an optimum pH around 9. We found another enzyme hydrolyzing anandamide in a human megakaryoblastic cell line (CMK). The enzyme present in the 12 000 x g pellet of the cell homogenate was solubilized by freeze-thaw, The solubilized enzyme showed an optimal pH around 5, and was almost inactive at alkaline pH, The enzyme activity was increased by the addition of dithiothreitol, In contrast, anandamide amidohydrolase of RBL-1 cells was mostly insoluble even after freeze-thaw, showed an optimal pH at 9, and was not affected by dithiothreitol, Furthermore, the enzyme of CMK cells was much less sensitive to phenylmethylsulfonyl fluoride and methyl arachidonoyl fluorophosphonate potently inhibiting anandamide amidohydrolase, and effectively hydrolyzed palmitoylethanolamide, which was a poor substrate for anandamide amidohydrolase. Thus, the enzyme of CMK cells is distinguishable from anandamide amidohydrolase. (C) 1999 Federation of European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 20:55:27